Isolation, crystallization and preliminary X-ray diffraction analysis of L-amino-acid oxidase from Vipera ammodytes ammodytes venom.
L-Amino-acid oxidase from the venom of Vipera ammodytes ammodytes, the most venomous snake in Europe, was isolated and crystallized using the sitting-drop vapour-diffusion method. The solution conditions under which the protein sample was monodisperse were optimized using dynamic light scattering prior to crystallization. The crystals belonged to space group C2, with unit-cell parameters a = 198.37, b = 96.38, c = 109.11 A, beta = 92.56 degrees . Initial diffraction data were collected to 2.6 A resolution. The calculated Matthews coefficient is approximately 2.6 A(3) Da(-1) assuming the presence of four molecules in the asymmetric unit.
Georgieva
Dessislava
D
Institute of Biochemistry and Molecular Biology, University of Hamburg, c/o DESY, Gebäude 22a, Notkestrasse 85, 22603 Hamburg, Germany.
Kardas
Anna
A
Buck
Friedrich
F
Perbandt
Markus
M
Betzel
Christian
C
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D050830:L-Amino Acid Oxidase / Q000737:chemistry* / Q000302:isolation & purification; D012996:Solutions; D014757:Viper Venoms / Q000737:chemistry* / Q000302:isolation & purification; D017819:Viperidae; D014961:X-Ray Diffraction / Q000379:methods
D012996:Solutions; D014757:Viper Venoms; D050830:L-Amino Acid Oxidase